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KMID : 0380019940090050525
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Korean Journal of Biotechnology and Bioengineering
1994 Volume.9 No. 5 p.525 ~ p.531
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Stabilization of Tyrosinase for Catechol Production
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Abstract
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Tyrosinase has two types of enzymatic activites, cresolase catalyzing the hydroxylation of monophenol and catecholase catalyzing the oxidation of o-phenol. Gradual inactivation of the enzyme during the reaction is a barrier to be overcome for the commercial application of the enzyme. Tyrosinase was stabilized by modifying the lysine residue of the enzyme using glutaraldehyde. In addition to that, tyrosinase was also stabilized by adapting the continuous reactor system. In packed bed reactor quinone could be easily removed, so the stability of tyrosinase increased. Borate buffer retarded the reaction rate of catechol to quinone and consequently decreased the tyrosinase inactivation. Tyrosinase immobilized on controlled pore glass showed significantly enhanced stability in a packed-bed reactor.
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